ID   GSPG_KLEPN              Reviewed;         140 AA.
AC   P15746;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   RecName: Full=Type II secretion system core protein G;
DE            Short=T2SS core protein G;
DE   AltName: Full=General secretion pathway protein G;
DE   AltName: Full=Pullulanase secretion protein PulG;
DE   Flags: Precursor;
GN   Name=pulG;
OS   Klebsiella pneumoniae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=UNF 5023;
RX   PubMed=2129543; DOI=10.1007/bf00633815;
RA   Reyss I., Pugsley A.P.;
RT   "Five additional genes in the pulC-O operon of the Gram-negative bacterium
RT   Klebsiella oxytoca UNF5023 which are required for pullulanase secretion.";
RL   Mol. Gen. Genet. 222:176-184(1990).
CC   -!- FUNCTION: Core component of the type II secretion system required for
CC       the energy-dependent secretion of extracellular factors such as
CC       proteases and toxins from the periplasm. Pseudopilin (pilin-like)
CC       protein that polymerizes to form the pseudopilus. Further
CC       polymerization triggers pseudopilus growth.
CC       {ECO:0000250|UniProtKB:Q00514}.
CC   -!- SUBUNIT: Type II secretion system is composed of four main components:
CC       the outer membrane complex, the inner membrane complex, the cytoplasmic
CC       secretion ATPase and the periplasm-spanning pseudopilus. Forms
CC       homomultimers. {ECO:0000250|UniProtKB:Q00514}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:Q00514}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- PTM: Cleaved by the prepilin peptidase. {ECO:0000250|UniProtKB:Q00514}.
CC   -!- PTM: Methylated by prepilin peptidase at the amino group of the N-
CC       terminal phenylalanine once the leader sequence is cleaved.
CC       {ECO:0000250|UniProtKB:Q00514}.
CC   -!- SIMILARITY: Belongs to the GSP G family. {ECO:0000305}.
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DR   EMBL; M32613; AAA25129.1; -; Genomic_DNA.
DR   PDB; 1T92; X-ray; 1.60 A; A/B=31-138.
DR   PDBsum; 1T92; -.
DR   AlphaFoldDB; P15746; -.
DR   SMR; P15746; -.
DR   TCDB; 3.A.15.1.1; the outer membrane protein secreting main terminal branch (mtb) family.
DR   EvolutionaryTrace; P15746; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015627; C:type II protein secretion system complex; IEA:InterPro.
DR   GO; GO:0015628; P:protein secretion by the type II secretion system; IEA:InterPro.
DR   Gene3D; 3.30.700.10; Glycoprotein, Type 4 Pilin; 1.
DR   InterPro; IPR000983; Bac_GSPG_pilin.
DR   InterPro; IPR012902; N_methyl_site.
DR   InterPro; IPR045584; Pilin-like.
DR   InterPro; IPR013545; T2SS_protein-GspG_C.
DR   InterPro; IPR010054; Type2_sec_GspG.
DR   NCBIfam; TIGR02532; IV_pilin_GFxxxE; 1.
DR   NCBIfam; TIGR01710; typeII_sec_gspG; 1.
DR   PANTHER; PTHR30093; GENERAL SECRETION PATHWAY PROTEIN G; 1.
DR   PANTHER; PTHR30093:SF44; TYPE II SECRETION SYSTEM CORE PROTEIN G-RELATED; 1.
DR   Pfam; PF07963; N_methyl; 1.
DR   Pfam; PF08334; T2SSG; 1.
DR   PRINTS; PR00813; BCTERIALGSPG.
DR   SUPFAM; SSF54523; Pili subunits; 1.
DR   PROSITE; PS00409; PROKAR_NTER_METHYL; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell inner membrane; Cell membrane; Membrane; Methylation;
KW   Protein transport; Transmembrane; Transmembrane helix; Transport.
FT   PROPEP          1..6
FT                   /note="Leader sequence"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT                   /id="PRO_0000449508"
FT   CHAIN           7..140
FT                   /note="Type II secretion system core protein G"
FT                   /id="PRO_0000024207"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          120..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         7
FT                   /note="N-methylphenylalanine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT   HELIX           33..60
FT                   /evidence="ECO:0007829|PDB:1T92"
FT   TURN            66..68
FT                   /evidence="ECO:0007829|PDB:1T92"
FT   HELIX           70..73
FT                   /evidence="ECO:0007829|PDB:1T92"
FT   STRAND          78..81
FT                   /evidence="ECO:0007829|PDB:1T92"
FT   TURN            88..91
FT                   /evidence="ECO:0007829|PDB:1T92"
FT   STRAND          92..94
FT                   /evidence="ECO:0007829|PDB:1T92"
FT   STRAND          105..107
FT                   /evidence="ECO:0007829|PDB:1T92"
FT   HELIX           111..113
FT                   /evidence="ECO:0007829|PDB:1T92"
FT   STRAND          116..119
FT                   /evidence="ECO:0007829|PDB:1T92"
FT   STRAND          122..124
FT                   /evidence="ECO:0007829|PDB:1T92"
FT   STRAND          127..129
FT                   /evidence="ECO:0007829|PDB:1T92"
FT   STRAND          135..137
FT                   /evidence="ECO:0007829|PDB:1T92"
SQ   SEQUENCE   140 AA;  15373 MW;  44264C2B5AA369B0 CRC64;
     MQRQRGFTLL EIMVVIVILG VLASLVVPNL MGNKEKADRQ KVVSDLVALE GALDMYKLDN
     SRYPTTEQGL QALVSAPSAE PHARNYPEGG YIRRLPQDPW GSDYQLLSPG QHGQVDIFSL
     GPDGVPESND DIGNWTIGKK
//